Species : |
Human |
Source : |
E.coli |
Tag : |
His |
Protein Length : |
Glu138~Val423 |
Description : |
Carboxypeptidases are enzymes that hydrolyze C-terminal peptide bonds. The carboxypeptidase family includes metallo-, serine, and cysteine carboxypeptidases. According to their substrate specificity, these enzymes are referred to as carboxypeptidase A (cleaving aliphatic residues) or carboxypeptidase B (cleaving basic amino residues). The protein encoded by this gene is activated by trypsin and acts on carboxypeptidase B substrates. After thrombin activation, the mature protein downregulates fibrinolysis. Polymorphisms have been described for this gene and its promoter region. Alternate splicing results in multiple transcript variants. |
Form : |
Freeze-dried powder |
Molecular Mass : |
Predicted Molecular Mass: 34.5kDa |
Endotoxin : |
<1.0EU per 1µg (determined by the LAL method) |
Purity : |
>95% |
Characteristic : |
The isoelectric point is 8.5. |
Applications : |
SDS-PAGE; WB; ELISA; IP |
Stability : |
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37°C for 48h, and no obvious degradation and precipitation were observed. The loss rate is less than 5% within the expiration date under appropriate storage condition. |
Storage : |
Avoid repeated freeze/thaw cycles. Store at 2-8°C for one month. Aliquot and store at -80°C for 12 months. |
Storage buffer : |
Supplied as lyophilized form in PBS, pH7.4, containing 5% sucrose, 0.01% sarcosyl. |
Reconstitution : |
Reconstitute in sterile PBS, pH7.2-pH7.4. |